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UniProtKB/Swiss-Prot O95831: Variant p.Gly308Glu

Apoptosis-inducing factor 1, mitochondrial
Gene: AIFM1
Variant information

Variant position:  308
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Glycine (G) to Glutamate (E) at position 308 (G308E, p.Gly308Glu).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from glycine (G) to medium size and acidic (E)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  In COXPD6; with prenatal ventriculomegaly and severe postnatal encephalomyopathy; no effect on redox potential; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding; decreased interaction with CHCHDE.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  308
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  613
The length of the canonical sequence.

Location on the sequence:   GDFRSLEKISREVKSITIIG  G GFLGSELACALGRKARALGT
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.

Residue conservation: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         GDFRSLEKISRE-VKSITIIGGGFLGSELACALGRKARAL-GT

Mouse                         GDFRALEKISRE-VKSITVIGGGFLGSELACALGRKSQAS-

Rat                           GDFRALEKISRE-VKSITVIGGGFLGSELACALGRKSQAS-

Drosophila                    DDFDRLRKLAAE-KRSITIVGNGFIGSELACSLAHYSRENN

Slime mold                    EDFRKLYEVVKDGGKHVTVLGGGFLGSELTCAINSNFQDK-

Sequence annotation in neighborhood:  
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.

TypePositionsDescription
Chain 102 – 613 Apoptosis-inducing factor 1, mitochondrial
Nucleotide binding 308 – 311 NAD 1
Region 134 – 483 FAD-dependent oxidoreductase
Modified residue 292 – 292 Phosphoserine
Alternative sequence 1 – 352 Missing. In isoform 5.
Alternative sequence 36 – 322 Missing. In isoform 2.
Alternative sequence 44 – 613 Missing. In isoform 6.


Literature citations

Interaction between AIF and CHCHD4 Regulates Respiratory Chain Biogenesis.
Hangen E.; Feraud O.; Lachkar S.; Mou H.; Doti N.; Fimia G.M.; Lam N.V.; Zhu C.; Godin I.; Muller K.; Chatzi A.; Nuebel E.; Ciccosanti F.; Flamant S.; Benit P.; Perfettini J.L.; Sauvat A.; Bennaceur-Griscelli A.; Ser-Le Roux K.; Gonin P.; Tokatlidis K.; Rustin P.; Piacentini M.; Ruvo M.; Blomgren K.; Kroemer G.; Modjtahedi N.;
Mol. Cell 58:1001-1014(2015)
Cited for: FUNCTION; INTERACTION WITH CHCHD4; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT COXPD6 GLU-308; CHARACTERIZATION OF VARIANT CMTX4 VAL-493;

Structure/Function Relations in AIFM1 Variants Associated with Neurodegenerative Disorders.
Sevrioukova I.F.;
J. Mol. Biol. 428:3650-3665(2016)
Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 103-613 IN COMPLEX WITH FAD; CHARACTERIZATION OF VARIANT SER-262; CHARACTERIZATION OF VARIANTS COXPD6 LEU-243; GLU-308 AND GLU-338; FUNCTION; DNA-BINDING; FAD-BINDING; CATALYTIC ACTIVITY; COFACTOR;

Early prenatal ventriculomegaly due to an AIFM1 mutation identified by linkage analysis and whole exome sequencing.
Berger I.; Ben-Neriah Z.; Dor-Wolman T.; Shaag A.; Saada A.; Zenvirt S.; Raas-Rothschild A.; Nadjari M.; Kaestner K.H.; Elpeleg O.;
Mol. Genet. Metab. 104:517-520(2011)
Cited for: VARIANT COXPD6 GLU-308;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.